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Entry version 85 (18 Sep 2019)
Sequence version 2 (07 Feb 2006)
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Protein

D-lysergyl-peptide-synthetase subunit 1

Gene

lpsA

Organism
Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii)
Status
Reviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

D-lysergyl-peptide-synthetase subunit 1; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid ergovaline, the predominant ergopeptine product in E.festucae var. lolii (PubMed:17308187). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD+, resulting in the formation of chanoclavine-I aldehyde (By similarity). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity). The presence of easA is not required to complete this reaction (By similarity). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (By similarity). Paspalic acid is then further converted to D-lysergic acid (By similarity). Ergovaline is assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a trimodular (lpsA) nonribosomal peptide synthetase subunit (PubMed:17308187, PubMed:11592979).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: ergot alkaloid biosynthesis

This protein is involved in the pathway ergot alkaloid biosynthesis, which is part of Alkaloid biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway ergot alkaloid biosynthesis and in Alkaloid biosynthesis.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLigase, Transferase

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00327

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
D-lysergyl-peptide-synthetase subunit 11 Publication (EC:2.3.1.-1 Publication)
Short name:
LPSA1 Publication
Alternative name(s):
Ergot alkaloid synthesis protein lpsA1 Publication
Nonribosomal peptide synthetase lpsA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:lpsA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEpichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri73839 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesClavicipitaceaeEpichloe

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Abolishes the production of ergovaline (PubMed:11592979).1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004391071 – 3589D-lysergyl-peptide-synthetase subunit 1Add BLAST3589

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei915O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2006O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei3096O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q96V34

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini883 – 952Carrier 1PROSITE-ProRule annotationAdd BLAST70
Domaini1974 – 2042Carrier 2PROSITE-ProRule annotationAdd BLAST69
Domaini3064 – 3132Carrier 3PROSITE-ProRule annotationAdd BLAST69

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni344 – 742Adenylation (A) domain 1Sequence analysisAdd BLAST399
Regioni995 – 1380Condensation (C) domain 1Sequence analysisAdd BLAST386
Regioni1424 – 1826Adenylation (A) domain 2Sequence analysisAdd BLAST403
Regioni2087 – 2509Condensation (C) domain 2Sequence analysisAdd BLAST423
Regioni2534 – 2929Adenylation (A) domain 3Sequence analysisAdd BLAST396
Regioni3187 – 3585Cyclization (Cyc) domainSequence analysisAdd BLAST399

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) or reductase domain (R) that releases the newly synthesized peptide from the enzyme (By similarity). LpsA1 has a domain arrangement (A-T-C-A-T-C-A-T-Cyc) with 3 A and 3 peptidyl carrier (PCP/T) domains, 2 C-domains, and a terminal domain called the Cyc domain (By similarity). The Cyc domain has limited similarity to both C and Cy domains of NRPS but is most different in the so-called C3 and Cy3 motif of the latter domains, suggesting a special mechanism in acyl diketopiperazine formation, which is the final step of D-lysergyl peptide lactam synthesis (By similarity). LpsA misses an N-terminal C domain in the first module, leading to the conclusion that this C domain is located on the other subunit (lpsB) containing the D-lysergic acid module (By similarity).By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NRP synthase family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 3 hits
3.30.559.10, 3 hits
3.40.50.12780, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010071 AA_adenyl_domain
IPR036736 ACP-like_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR023213 CAT-like_dom_sf
IPR001242 Condensatn
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00501 AMP-binding, 3 hits
PF00668 Condensation, 4 hits
PF00550 PP-binding, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00823 PKS_PP, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336 SSF47336, 3 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01733 AA-adenyl-dom, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 3 hits
PS00012 PHOSPHOPANTETHEINE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q96V34-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSTTVEPVG STYARPKPLG NLDHRIEQLL GSESVLNESP GHSPNAYGIP
60 70 80 90 100
YTARNLTLED VDHCKSLTNK DLSLEFWKSH LQTAKPCILT RLKPGTGSSI
110 120 130 140 150
LSSRQSVKVD LGGVNTTCRN LFDSTGISLM TVFKVAWGMV LSTYTGSDHV
160 170 180 190 200
CFGYGAARPS MSVDGEQTTI KPLIKMLPCD MLFKGGTTLL GTVHKAESDF
210 220 230 240 250
ICTIPYQSVS IAEIHHGIGT ESGALFNTSI IFWPQEDFSD NPITEVLSQK
260 270 280 290 300
VTETESLTEC DIIMHVDSKQ QCYLSYWDYF LSDEQANHLA GALNVAMKSI
310 320 330 340 350
FESPHRPVGQ VEMFSYLDQQ KLLQWNGQAP IASESCLGDL IGQNCHSRPD
360 370 380 390 400
SLAVDSWDGF FTYQELDRLS STLANKLRCA GVGPDVFVTA CFDRCKWMPV
410 420 430 440 450
AMLGIIKAGG AICALDPSYP LGRLTGMCQL LKSTVVLTTA NNAQQAEQLA
460 470 480 490 500
LTTIVLGNDL WTGDSYDEQE RQAPLSNVCP SNALYAVFTS GSTGKPKGVV
510 520 530 540 550
VEHRSFSSCA LASLKPLDIR PHDRVLHISS YAFDISIFET LATLTAGASV
560 570 580 590 600
AIPSEKARRE DLPGAMRELQ ATWAFLTPTV ARMYQPKDFP SLRTLCLGGE
610 620 630 640 650
AIHTSDIGLW ASKNLVTGYN PAESCPLGIS GPADKSAASF LGWSFSSQAS
660 670 680 690 700
WIVDPRDYQK LAPIGAVGEL MIEGPAVARG YIHDLTCSHP DSPFVLPPPQ
710 720 730 740 750
WLSRFRASTS QDTRLYRTGD LVQYGSNGSV HFIGRKDLQV KVHGQRVELS
760 770 780 790 800
EIEFQLHKTL LPLDCKVVVD AVTFTGHTSV IAFITAAEHS DLENEDDAVR
810 820 830 840 850
SPDVKVITQD FEIRAADAAT KLQSILPRHM VPTIYLPVGH IPMSRSGKID
860 870 880 890 900
RQKLRSLALS LPRETLYHIG RQPGPGEIVV TDVERRLQLL FAQVLDLSPE
910 920 930 940 950
KIKADSDFFR LGGDSIYAMK LLALAPQQGP RDLTYEEIFR HPKLRDLAAA
960 970 980 990 1000
SSSFSNISLA IPEDLGPAPF SLARDADSLT KIASEQCGVA VGDIEDIYPC
1010 1020 1030 1040 1050
TSLQESLIAS TAHDQDAYVG VQSFTLNDDI DTTRLKMAWK MTSEGHPILR
1060 1070 1080 1090 1100
TRIIQTDSGA PYQAVIRGPL SWSEESSSDD LPPQFQPSIG LGTPLVQLCL
1110 1120 1130 1140 1150
TNSRLLVAMH HALYDGWSLP LLLAEVDQAY RQLSVRQLPP FNRYVKHVTE
1160 1170 1180 1190 1200
TVDSAASFWK AELQDADPVD FPPLPHLNYK PEPRALLTKS ITLTAHTNSQ
1210 1220 1230 1240 1250
HNVTLATELQ LAWALTSHTY TNSQDVVFGI ISSGRGAPVA GIERMLGPTF
1260 1270 1280 1290 1300
ASTPLRVPLD PAQDVREALE ELQYRLAEQT KYVQIGLQRI RQQGPNAAAA
1310 1320 1330 1340 1350
CSFQTMLVVE PNQPVKTQSA WFSRHEFLSE LTRFSSHSLT LRCKLLAGSV
1360 1370 1380 1390 1400
EVTAIYDQLV VPDAQMQRIL SQFQHILTQI QGIGSRDTTI GDIDRLSSGD
1410 1420 1430 1440 1450
WNELQAWNST LPPGLELSVH QMVQAKAQMQ PEALAIHSWD GDLTYKELED
1460 1470 1480 1490 1500
YAKGLANRLH ALGVRPNTFV AIYLQKSLWV VVAQLAVLIA GAAFTTLETS
1510 1520 1530 1540 1550
QPINRLRDVC RTVQPTVVLT SDKLRLSGAD LEVPAPLLVI NQQLLLEEPG
1560 1570 1580 1590 1600
SHSRPLENHT IMASDAMYSI ATSGTTGKPK VVVIEHQAFL ANSKHLIDRW
1610 1620 1630 1640 1650
GFTADSRVLQ FAGYSFDAMI VEHFITLLAG GCICIPSSFD RDNRLATCIV
1660 1670 1680 1690 1700
EMRVNWAMLT SSVIPLFTPA AVPTLQTLVQ AGEPMHQGIT DCWASHVQLF
1710 1720 1730 1740 1750
NAYGPTECSV ISTTSNIINP DARNPRNIGF TTGGVCWIVD PENPESPPVP
1760 1770 1780 1790 1800
IGAEGELIIE GAILARGYLG DRVRTAAAFT LRPGWLDDFR GSSGDNRIYR
1810 1820 1830 1840 1850
TGDIVRYDPD GSISYVRRKD SQVKLRGQRV ELLDVEHHLQ NCFPGALQVV
1860 1870 1880 1890 1900
ADIVTVPNTQ SSALVALVLA TPTSSSSVAI ESCSNDDQAT TAHGLLLLAN
1910 1920 1930 1940 1950
NPQFLIDASA AELALQDRVP SYMVPSLFIP TSRFPRDVSG KVNRGEITRS
1960 1970 1980 1990 2000
LAALSRQEWD GYVSTNRVAP TSGLERELQK IWARILNIPP DTIGVHDSFF
2010 2020 2030 2040 2050
RLGGDSITCM QVAAQCSRTG ILITVKDIFK RRTIEKLAAA AVVVQCPESS
2060 2070 2080 2090 2100
TTERVNTAEA KFSFYGPGQL EEYMIQIQPQ LGEGQVVEDI YPCSPIQRGI
2110 2120 2130 2140 2150
LMSHARNSGN YEEVIQWKVI SRAPVDVCRL RDAWAQVVDR HAVLRTLFLH
2160 2170 2180 2190 2200
VCKENYLDQV VLRSHSPMVL VYNEGEEPVN PVSTGCSQPM HHLRVKRSSA
2210 2220 2230 2240 2250
GGITVRLHIN HALVDGASLF IIRRDLAMAY EGRLASSRAS SPYRDYIAYL
2260 2270 2280 2290 2300
QNCHSQIQSN EYWQSYMEGT APCLFPTLKN AGAQDSQQPF EAFTLQLGAT
2310 2320 2330 2340 2350
ADLNQFCENH RLALTSVLHV VWAMVVQRYT AMDEVCFGYM TSGRHVPVAG
2360 2370 2380 2390 2400
VQDIVGPLFN MLVARVGLPH DATLLSVMQK YHDNFLISLD HQHQSLAETL
2410 2420 2430 2440 2450
HSIGSASGEL FNTLVSIFND QREGEPAHKS SAVTLVGDDI HSRSEYAITL
2460 2470 2480 2490 2500
NVLMLADQVH IQLSYHTSWL SDNYARMIAE TFRHVLATVL GQPQLRLNEI
2510 2520 2530 2540 2550
EMLDEEHRSG LYGRNHAAVP SFDSCIHYTI HQRCLESPES PAICAWDGDF
2560 2570 2580 2590 2600
SYRRLDQLSS SLAEELIGHG VGVEMTIPVL LEKTCWTPVA MLAVLKSGAS
2610 2620 2630 2640 2650
FVLMDASHPL GRLQTICEAI NPPVILASPQ TRSKAVGLTS HVIEVTNRLL
2660 2670 2680 2690 2700
EQEQAEQQQT WPRVVTKGSN AAYVVFTSGS TGKPKGAIVD HSCLATAAGH
2710 2720 2730 2740 2750
LPSRMYINSA SRVLQFSSHA WDIPVTDVLL TLRVGGCVCI PSDEERIGNL
2760 2770 2780 2790 2800
AQVANRMMVN WALLTPTVAR LVKPEDFTHL QTLVLAGEAV SSTDLTTWHD
2810 2820 2830 2840 2850
KVRLIQGYGP AECSLVSTVS EPLTPSDNPR NIGQPNGCVA WVVHRDNHHL
2860 2870 2880 2890 2900
LAPSGAIEEL VLEGPIVSRG YINDPERSAA VFVDPPTWLT RLRGGHSPTR
2910 2920 2930 2940 2950
LYKTGDLVSA GLDGCLSFVG RKDDQVKIRG QRVELGEVEA LASQAFPGSH
2960 2970 2980 2990 3000
VVVETVKDLS STILVAFILQ KETAHAQPSS ISSLLHPPSP LFRELISAAS
3010 3020 3030 3040 3050
CSLRETMPSF MIPTVFLPLA HLPKAPTGKT DRKFLRGHVA SLSRMELEAY
3060 3070 3080 3090 3100
SIVDATGRAP STPLETRLQE LVGRVLHRSP ESIPLDEDLF TFGLDSLTAM
3110 3120 3130 3140 3150
TLATLVREDG LAISVPTIFQ RPRLSELAVV LNQEQQIKQG QFLAPPPNAL
3160 3170 3180 3190 3200
MASMDELCAQ WQLDRSQVVN IAPTTYYQRG SLASHHTNFI ALHFSQPLDP
3210 3220 3230 3240 3250
IPFRNAVVGL VQKHAILRTA FVPFRETFVQ LILRDFDLPV QEIRTDEDDP
3260 3270 3280 3290 3300
SVVAESFCRE ADRVPVSFGT PITQLYMILG RAGDRLSAVL RLQRAQYDGV
3310 3320 3330 3340 3350
AVSCMIADLR SAFDEAPSSA LPTLEYADYV ISRRAHSSPP VFQVWRELLQ
3360 3370 3380 3390 3400
GSSMTYLVPP TEYIRSTDRS RTELLVTSSC DIPMPDTKGG ITMATVIKTA
3410 3420 3430 3440 3450
WALCLARQTQ SKDVVFAQLV RNRHLAIAGI DRTVGPCINY VPVRASLNLD
3460 3470 3480 3490 3500
WTAKEFLHWV QRQHIRTMTC DMADWDDLVI ESTSWPRDTE LGSAVHYLSA
3510 3520 3530 3540 3550
PVASDYTFAG DVPCQFQMYD FKMVHTYPMV TCLPFPSVGD SSLTVLKIIL
3560 3570 3580
TSAVFGQGVA DRLLSLFRDM VHRLTTYPES LVSELLIIR
Length:3,589
Mass (Da):394,889
Last modified:February 7, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8B8051761A23841B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF368420 Genomic DNA Translation: AAL26315.2

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF368420 Genomic DNA Translation: AAL26315.2

3D structure databases

SMRiQ96V34
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00327

Family and domain databases

Gene3Di1.10.1200.10, 3 hits
3.30.559.10, 3 hits
3.40.50.12780, 3 hits
InterProiView protein in InterPro
IPR010071 AA_adenyl_domain
IPR036736 ACP-like_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR023213 CAT-like_dom_sf
IPR001242 Condensatn
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
PfamiView protein in Pfam
PF00501 AMP-binding, 3 hits
PF00668 Condensation, 4 hits
PF00550 PP-binding, 3 hits
SMARTiView protein in SMART
SM00823 PKS_PP, 3 hits
SUPFAMiSSF47336 SSF47336, 3 hits
TIGRFAMsiTIGR01733 AA-adenyl-dom, 2 hits
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 3 hits
PS00012 PHOSPHOPANTETHEINE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLPSA1_EPIFI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q96V34
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2017
Last sequence update: February 7, 2006
Last modified: September 18, 2019
This is version 85 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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